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Magnesium in PDB 5eik: Structure of A Trimeric Intracellular Cation Channel From C. Elegans in the Absence of CA2+

Protein crystallography data

The structure of Structure of A Trimeric Intracellular Cation Channel From C. Elegans in the Absence of CA2+, PDB code: 5eik was solved by M.H.Hu, H.T.Yang, Z.F.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.30
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 126.340, 126.340, 135.570, 90.00, 90.00, 120.00
R / Rfree (%) 21.4 / 24.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Trimeric Intracellular Cation Channel From C. Elegans in the Absence of CA2+ (pdb code 5eik). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of A Trimeric Intracellular Cation Channel From C. Elegans in the Absence of CA2+, PDB code: 5eik:

Magnesium binding site 1 out of 1 in 5eik

Go back to Magnesium Binding Sites List in 5eik
Magnesium binding site 1 out of 1 in the Structure of A Trimeric Intracellular Cation Channel From C. Elegans in the Absence of CA2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Trimeric Intracellular Cation Channel From C. Elegans in the Absence of CA2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg303

b:92.1
occ:1.00
O A:HOH480 2.4 60.1 1.0
O A:HOH461 2.4 0.8 1.0
O A:HOH463 2.8 0.2 1.0
CE1 A:HIS136 3.0 51.2 1.0
NE2 A:HIS136 3.1 49.1 1.0
O A:HOH482 3.5 82.0 1.0
CB A:ALA140 4.3 32.2 1.0
ND1 A:HIS136 4.3 48.9 1.0
CD2 A:HIS136 4.4 48.4 1.0
O A:ACT306 4.4 0.5 1.0
C A:ACT306 4.5 0.5 1.0
OXT A:ACT306 4.8 0.9 1.0
O A:HOH478 4.9 61.0 1.0
O A:HOH432 4.9 53.0 1.0
O A:HOH467 4.9 69.2 1.0
CH3 A:ACT306 5.0 0.1 1.0

Reference:

H.T.Yang, M.H.Hu, J.L.Guo, X.M.Ou, T.X.Cai, Z.F.Liu. Pore Architecture of Tric Channels and Insights Into Their Gating Mechanism Nature 2016.
ISSN: ESSN 1476-4687
DOI: 10.1038/NATURE19767
Page generated: Sun Sep 29 03:49:48 2024

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